TUT7_HUMAN
ID TUT7_HUMAN Reviewed; 1495 AA.
AC Q5VYS8; Q5H9T0; Q5VYS5; Q5VYS7; Q658Z9; Q659A2; Q6MZJ3; Q8N5F0; Q96N57;
AC Q96NE8; Q9C0F2; Q9H8M6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Terminal uridylyltransferase 7 {ECO:0000305};
DE Short=TUTase 7 {ECO:0000305};
DE EC=2.7.7.52 {ECO:0000269|PubMed:17353264};
DE AltName: Full=Zinc finger CCHC domain-containing protein 6;
GN Name=TUT7 {ECO:0000312|HGNC:HGNC:25817};
GN Synonyms=HS2, KIAA1711, ZCCHC6 {ECO:0000312|HGNC:HGNC:25817};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Cervix, Endometrial tumor, Fetal kidney, and Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1385 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1019-1495 (ISOFORM 6).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1495 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [6]
RP ABSENCE OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT 5'.";
RL Genes Dev. 22:50-65(2008).
RN [7]
RP CATALYTIC ACTIVITY.
RX PubMed=17353264; DOI=10.1128/mcb.02209-06;
RA Rissland O.S., Mikulasova A., Norbury C.J.;
RT "Efficient RNA polyuridylation by noncanonical poly(A) polymerases.";
RL Mol. Cell. Biol. 27:3612-3624(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-64; SER-172 AND
RP SER-844, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION.
RX PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
RA Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H., Han J.,
RA Kim V.N.;
RT "TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through pre-
RT microRNA uridylation.";
RL Cell 138:696-708(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION IN PRE-LET-7 URIDYLATION.
RX PubMed=22898984; DOI=10.1261/rna.034538.112;
RA Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.;
RT "Lin28-mediated control of let-7 microRNA expression by alternative TUTases
RT Zcchc11 (TUT4) and Zcchc6 (TUT7).";
RL RNA 18:1875-1885(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64 AND SER-600, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25480299; DOI=10.1016/j.cell.2014.10.055;
RA Lim J., Ha M., Chang H., Kwon S.C., Simanshu D.K., Patel D.J., Kim V.N.;
RT "Uridylation by TUT4 and TUT7 marks mRNA for degradation.";
RL Cell 159:1365-1376(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP FUNCTION.
RX PubMed=25979828; DOI=10.15252/embj.201590931;
RA Kim B., Ha M., Loeff L., Chang H., Simanshu D.K., Li S., Fareh M.,
RA Patel D.J., Joo C., Kim V.N.;
RT "TUT7 controls the fate of precursor microRNAs by using three different
RT uridylation mechanisms.";
RL EMBO J. 34:1801-1815(2015).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MOV10, AND MUTAGENESIS OF
RP ASP-1060.
RX PubMed=30122351; DOI=10.1016/j.cell.2018.07.022;
RA Warkocki Z., Krawczyk P.S., Adamska D., Bijata K., Garcia-Perez J.L.,
RA Dziembowski A.;
RT "Uridylation by TUT4/7 Restricts Retrotransposition of Human LINE-1s.";
RL Cell 0:0-0(2018).
RN [20] {ECO:0007744|PDB:5W0B, ECO:0007744|PDB:5W0M, ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 983-1365 IN COMPLEX WITH DSRNA;
RP UTP AND ZINC, FUNCTION, DOMAIN, AND MUTAGENESIS OF 1097-LEU--ILE-1099.
RX PubMed=28671666; DOI=10.1038/nsmb.3428;
RA Faehnle C.R., Walleshauser J., Joshua-Tor L.;
RT "Multi-domain utilization by TUT4 and TUT7 in control of let-7
RT biogenesis.";
RL Nat. Struct. Mol. Biol. 24:658-665(2017).
CC -!- FUNCTION: Uridylyltransferase that mediates the terminal uridylation of
CC mRNAs with short (less than 25 nucleotides) poly(A) tails, hence
CC facilitating global mRNA decay (PubMed:19703396, PubMed:25480299).
CC Essential for both oocyte maturation and fertility. Through 3' terminal
CC uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by
CC eliminating transcripts during oocyte growth (By similarity). Involved
CC in microRNA (miRNA)-induced gene silencing through uridylation of
CC deadenylated miRNA targets (PubMed:25480299). Also functions as an
CC integral regulator of microRNA biogenesiS using 3 different uridylation
CC mechanisms (PubMed:25979828). Acts as a suppressor of miRNA biogenesis
CC by mediating the terminal uridylation of some miRNA precursors,
CC including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is not
CC processed by Dicer and undergo degradation. Pre-let-7 uridylation is
CC strongly enhanced in the presence of LIN28A (PubMed:22898984). In the
CC absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs,
CC which includes most of pre-let7 members, that shapes an optimal 3' end
CC overhang for efficient processing (PubMed:25979828, PubMed:28671666).
CC Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may
CC promote rapid degradation of non-functional pre-miRNA species
CC (PubMed:25979828). Does not play a role in replication-dependent
CC histone mRNA degradation (PubMed:18172165). Due to functional
CC redundancy between TUT4 and TUT7, the identification of the specific
CC role of each of these proteins is difficult (PubMed:25979828,
CC PubMed:25480299, PubMed:19703396, PubMed:22898984, PubMed:18172165,
CC PubMed:28671666). TUT4 and TUT7 restrict retrotransposition of long
CC interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting
CC the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in
CC the cytoplasm which inhibits initiation of reverse transcription once
CC in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in
CC cytoplasmic ribonucleoprotein granules (PubMed:30122351).
CC {ECO:0000250|UniProtKB:Q5BLK4, ECO:0000269|PubMed:18172165,
CC ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22898984,
CC ECO:0000269|PubMed:25480299, ECO:0000269|PubMed:25979828,
CC ECO:0000269|PubMed:28671666, ECO:0000269|PubMed:30122351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000269|PubMed:17353264};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with MOV10; the interaction is RNA-dependent.
CC {ECO:0000269|PubMed:30122351}.
CC -!- INTERACTION:
CC Q5VYS8-5; P02489: CRYAA; NbExp=3; IntAct=EBI-9088812, EBI-6875961;
CC Q5VYS8-5; P14136: GFAP; NbExp=3; IntAct=EBI-9088812, EBI-744302;
CC Q5VYS8-5; O14908-2: GIPC1; NbExp=3; IntAct=EBI-9088812, EBI-25913156;
CC Q5VYS8-5; P28799: GRN; NbExp=3; IntAct=EBI-9088812, EBI-747754;
CC Q5VYS8-5; P04792: HSPB1; NbExp=3; IntAct=EBI-9088812, EBI-352682;
CC Q5VYS8-5; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-9088812, EBI-1055254;
CC Q5VYS8-5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9088812, EBI-10975473;
CC Q5VYS8-5; Q92876: KLK6; NbExp=3; IntAct=EBI-9088812, EBI-2432309;
CC Q5VYS8-5; P02545: LMNA; NbExp=3; IntAct=EBI-9088812, EBI-351935;
CC Q5VYS8-5; P19404: NDUFV2; NbExp=3; IntAct=EBI-9088812, EBI-713665;
CC Q5VYS8-5; P07196: NEFL; NbExp=3; IntAct=EBI-9088812, EBI-475646;
CC Q5VYS8-5; P35240: NF2; NbExp=3; IntAct=EBI-9088812, EBI-1014472;
CC Q5VYS8-5; Q96CV9: OPTN; NbExp=3; IntAct=EBI-9088812, EBI-748974;
CC Q5VYS8-5; P16284: PECAM1; NbExp=3; IntAct=EBI-9088812, EBI-716404;
CC Q5VYS8-5; P60891: PRPS1; NbExp=3; IntAct=EBI-9088812, EBI-749195;
CC Q5VYS8-5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-9088812, EBI-5235340;
CC Q5VYS8-5; P08670: VIM; NbExp=3; IntAct=EBI-9088812, EBI-353844;
CC Q5VYS8-5; O76024: WFS1; NbExp=3; IntAct=EBI-9088812, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25480299,
CC ECO:0000269|PubMed:30122351}. Note=Expression is pancytoplasmic in
CC contrast with TUT4 expression which is enriched in cytoplasmic
CC ribonucleoprotein granules. {ECO:0000269|PubMed:30122351}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q5VYS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VYS8-2; Sequence=VSP_013837, VSP_013838;
CC Name=3;
CC IsoId=Q5VYS8-3; Sequence=VSP_013835, VSP_013836;
CC Name=4;
CC IsoId=Q5VYS8-4; Sequence=VSP_013832, VSP_013839;
CC Name=5;
CC IsoId=Q5VYS8-5; Sequence=VSP_013833, VSP_013834;
CC Name=6;
CC IsoId=Q5VYS8-6; Sequence=VSP_013840;
CC -!- DOMAIN: Utilizes two multidomain functional modules during the switch
CC from monouridylation to oligouridylation. The catalytic module
CC (containing the 3 CCHC-type Zinc finger domains) is essential for both
CC activities while the Lin28-interacting module (LIM) at the N-termail
CC part is indispensable for oligouridylation.
CC {ECO:0000269|PubMed:28671666}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14584.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71052.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL832026; CAH56219.1; -; mRNA.
DR EMBL; AL832193; CAH56214.1; -; mRNA.
DR EMBL; BX641077; CAE46038.1; -; mRNA.
DR EMBL; CR933643; CAI45944.1; -; mRNA.
DR EMBL; CR933644; CAI45945.1; -; mRNA.
DR EMBL; CR936608; CAI56753.1; -; mRNA.
DR EMBL; AL137849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032456; AAH32456.1; -; mRNA.
DR EMBL; AK023471; BAB14584.1; ALT_INIT; mRNA.
DR EMBL; AK055546; BAB70951.1; -; mRNA.
DR EMBL; AK055948; BAB71052.1; ALT_INIT; mRNA.
DR EMBL; AB051498; BAB21802.1; -; mRNA.
DR CCDS; CCDS35057.1; -. [Q5VYS8-1]
DR CCDS; CCDS55323.1; -. [Q5VYS8-4]
DR RefSeq; NP_001171988.1; NM_001185059.1. [Q5VYS8-1]
DR RefSeq; NP_001172003.1; NM_001185074.1. [Q5VYS8-4]
DR RefSeq; NP_001317647.1; NM_001330718.1.
DR RefSeq; NP_078893.2; NM_024617.3. [Q5VYS8-1]
DR RefSeq; XP_016870619.1; XM_017015130.1. [Q5VYS8-1]
DR RefSeq; XP_016870620.1; XM_017015131.1. [Q5VYS8-1]
DR PDB; 5W0B; X-ray; 2.61 A; A/B/C=983-1365.
DR PDB; 5W0M; X-ray; 2.30 A; A/B/C=983-1365.
DR PDB; 5W0N; X-ray; 2.50 A; A/B/C=963-1365.
DR PDB; 5W0O; X-ray; 2.49 A; A/B=983-1365.
DR PDBsum; 5W0B; -.
DR PDBsum; 5W0M; -.
DR PDBsum; 5W0N; -.
DR PDBsum; 5W0O; -.
DR AlphaFoldDB; Q5VYS8; -.
DR SMR; Q5VYS8; -.
DR BioGRID; 122795; 131.
DR IntAct; Q5VYS8; 50.
DR STRING; 9606.ENSP00000365130; -.
DR iPTMnet; Q5VYS8; -.
DR PhosphoSitePlus; Q5VYS8; -.
DR BioMuta; ZCCHC6; -.
DR DMDM; 67462100; -.
DR EPD; Q5VYS8; -.
DR jPOST; Q5VYS8; -.
DR MassIVE; Q5VYS8; -.
DR MaxQB; Q5VYS8; -.
DR PaxDb; Q5VYS8; -.
DR PeptideAtlas; Q5VYS8; -.
DR PRIDE; Q5VYS8; -.
DR ProteomicsDB; 65642; -. [Q5VYS8-1]
DR ProteomicsDB; 65643; -. [Q5VYS8-2]
DR ProteomicsDB; 65644; -. [Q5VYS8-3]
DR ProteomicsDB; 65645; -. [Q5VYS8-4]
DR ProteomicsDB; 65646; -. [Q5VYS8-5]
DR ProteomicsDB; 65647; -. [Q5VYS8-6]
DR Antibodypedia; 13297; 45 antibodies from 13 providers.
DR DNASU; 79670; -.
DR Ensembl; ENST00000375960.6; ENSP00000365127.2; ENSG00000083223.18. [Q5VYS8-4]
DR Ensembl; ENST00000375963.8; ENSP00000365130.3; ENSG00000083223.18. [Q5VYS8-1]
DR GeneID; 79670; -.
DR KEGG; hsa:79670; -.
DR MANE-Select; ENST00000375963.8; ENSP00000365130.3; NM_024617.4; NP_078893.2.
DR UCSC; uc004aoq.4; human. [Q5VYS8-1]
DR CTD; 79670; -.
DR DisGeNET; 79670; -.
DR GeneCards; TUT7; -.
DR HGNC; HGNC:25817; TUT7.
DR HPA; ENSG00000083223; Low tissue specificity.
DR MIM; 613467; gene.
DR neXtProt; NX_Q5VYS8; -.
DR OpenTargets; ENSG00000083223; -.
DR PharmGKB; PA134971144; -.
DR VEuPathDB; HostDB:ENSG00000083223; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156859; -.
DR HOGENOM; CLU_003287_1_0_1; -.
DR InParanoid; Q5VYS8; -.
DR OMA; SKSDCMF; -.
DR OrthoDB; 803033at2759; -.
DR PhylomeDB; Q5VYS8; -.
DR TreeFam; TF315661; -.
DR BRENDA; 2.7.7.52; 2681.
DR PathwayCommons; Q5VYS8; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR SignaLink; Q5VYS8; -.
DR SIGNOR; Q5VYS8; -.
DR BioGRID-ORCS; 79670; 34 hits in 1082 CRISPR screens.
DR ChiTaRS; ZCCHC6; human.
DR GeneWiki; ZCCHC6; -.
DR GenomeRNAi; 79670; -.
DR Pharos; Q5VYS8; Tbio.
DR PRO; PR:Q5VYS8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VYS8; protein.
DR Bgee; ENSG00000083223; Expressed in tendon of biceps brachii and 190 other tissues.
DR ExpressionAtlas; Q5VYS8; baseline and differential.
DR Genevisible; Q5VYS8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070569; F:uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010586; P:miRNA metabolic process; IDA:UniProtKB.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IDA:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
DR GO; GO:0001556; P:oocyte maturation; ISS:UniProtKB.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
DR GO; GO:0071076; P:RNA 3' uridylation; IDA:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
DR Gene3D; 3.30.460.10; -; 2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 2.
DR Pfam; PF00098; zf-CCHC; 3.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57756; SSF57756; 3.
DR SUPFAM; SSF81301; SSF81301; 2.
DR PROSITE; PS50158; ZF_CCHC; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Magnesium; Manganese;
KW Metal-binding; Nucleotidyltransferase; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1495
FT /note="Terminal uridylyltransferase 7"
FT /id="PRO_0000150957"
FT DOMAIN 551..600
FT /note="PAP-associated 1"
FT DOMAIN 1233..1286
FT /note="PAP-associated 2"
FT ZN_FING 244..274
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT ZN_FING 963..980
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1345..1362
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047,
FT ECO:0000269|PubMed:28671666, ECO:0007744|PDB:5W0B,
FT ECO:0007744|PDB:5W0M, ECO:0007744|PDB:5W0N"
FT ZN_FING 1451..1468
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1495
FT /note="Sufficient for monouridylation activity"
FT /evidence="ECO:0000269|PubMed:25979828"
FT REGION 1367..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1047..1050
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O"
FT BINDING 1057..1060
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O"
FT BINDING 1058
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1060
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1130
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O"
FT BINDING 1152
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O"
FT BINDING 1170..1174
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O"
FT BINDING 1286
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BLK4"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BLK4"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 363..486
FT /note="MSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQSGLLCKVSAGNE
FT NACLTTKHLTALGKLEPKLVPLVIAFRYWAKLCSIDRPEEGGLPPYVFALMAIFFLQQR
FT KEPLLPVYLGSWI -> I (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013832"
FT VAR_SEQ 403..412
FT /note="SGLLCKVSAG -> RSHFFKLFIY (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013833"
FT VAR_SEQ 413..1495
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013834"
FT VAR_SEQ 538..544
FT /note="SLILDVK -> VSSLLCR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013835"
FT VAR_SEQ 545..1495
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013836"
FT VAR_SEQ 597..615
FT /note="DPYSVKRNVARTLNSQPVF -> GISKCLSYSPPLFFLKVPV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013837"
FT VAR_SEQ 616..1495
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013838"
FT VAR_SEQ 960..1072
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013839"
FT VAR_SEQ 1157..1194
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013840"
FT VARIANT 40
FT /note="A -> V (in dbSNP:rs2378695)"
FT /id="VAR_053753"
FT MUTAGEN 1060
FT /note="D->A: Abolishes inhibition of LIRE1
FT retrotransposition."
FT /evidence="ECO:0000269|PubMed:30122351"
FT MUTAGEN 1097..1099
FT /note="LPI->WPW: Abolishes monouridylation activity."
FT /evidence="ECO:0000269|PubMed:28671666"
FT CONFLICT 157
FT /note="K -> R (in Ref. 4; BAB70951)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="R -> T (in Ref. 1; CAE46038)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="S -> N (in Ref. 1; CAE46038)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="G -> V (in Ref. 1; CAI45944)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="Missing (in Ref. 1; CAI45944/CAH56219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="V -> M (in Ref. 1; CAH56219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="P -> S (in Ref. 1; CAH56219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1474
FT /note="G -> D (in Ref. 1; CAI45944)"
FT /evidence="ECO:0000305"
FT HELIX 995..1012
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1016..1034
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1040..1045
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1046..1048
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1059..1065
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1071..1073
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1076..1087
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1093..1099
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1101..1104
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1106..1111
FT /evidence="ECO:0007829|PDB:5W0M"
FT TURN 1112..1115
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1116..1123
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1125..1138
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1142..1158
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1163..1165
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1170..1183
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1184..1186
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1192..1194
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1197..1200
FT /evidence="ECO:0007829|PDB:5W0N"
FT HELIX 1217..1219
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1220..1223
FT /evidence="ECO:0007829|PDB:5W0M"
FT TURN 1225..1228
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1234..1247
FT /evidence="ECO:0007829|PDB:5W0M"
FT TURN 1251..1253
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1254..1256
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1266..1269
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1273..1275
FT /evidence="ECO:0007829|PDB:5W0B"
FT TURN 1288..1291
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1294..1312
FT /evidence="ECO:0007829|PDB:5W0M"
FT TURN 1316..1321
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1322..1324
FT /evidence="ECO:0007829|PDB:5W0O"
FT HELIX 1325..1329
FT /evidence="ECO:0007829|PDB:5W0M"
FT HELIX 1332..1335
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1344..1346
FT /evidence="ECO:0007829|PDB:5W0B"
FT TURN 1348..1350
FT /evidence="ECO:0007829|PDB:5W0M"
FT STRAND 1353..1355
FT /evidence="ECO:0007829|PDB:5W0B"
FT HELIX 1357..1359
FT /evidence="ECO:0007829|PDB:5W0M"
SQ SEQUENCE 1495 AA; 171229 MW; 1AAB0F5B37266FF9 CRC64;
MGDTAKPYFV KRTKDRGTMD DDDFRRGHPQ QDYLIIDDHA KGHGSKMEKG LQKKKITPGN
YGNTPRKGPC AVSSNPYAFK NPIYSQPAWM NDSHKDQSKR WLSDEHTGNS DNWREFKPGP
RIPVINRQRK DSFQENEDGY RWQDTRGCRT VRRLFHKDLT SLETTSEMEA GSPENKKQRS
RPRKPRKTRN EENEQDGDLE GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNYP
TAKYTCRLCD VLIESIAFAH KHIKEKRHKK NIKEKQEEEL LTTLPPPTPS QINAVGIAID
KVVQEFGLHN ENLEQRLEIK RIMENVFQHK LPDCSLRLYG SSCSRLGFKN SDVNIDIQFP
AIMSQPDVLL LVQECLKNSD SFIDVDADFH ARVPVVVCRE KQSGLLCKVS AGNENACLTT
KHLTALGKLE PKLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAIFFL QQRKEPLLPV
YLGSWIEGFS LSKLGNFNLQ DIEKDVVIWE HTDSAAGDTG ITKEEAPRET PIKRGQVSLI
LDVKHQPSVP VGQLWVELLR FYALEFNLAD LVISIRVKEL VSRELKDWPK KRIAIEDPYS
VKRNVARTLN SQPVFEYILH CLRTTYKYFA LPHKITKSSL LKPLNAITCI SEHSKEVINH
HPDVQTKDDK LKNSVLAQGP GATSSAANTC KVQPLTLKET AESFGSPPKE EMGNEHISVH
PENSDCIQAD VNSDDYKGDK VYHPETGRKN EKEKVGRKGK HLLTVDQKRG EHVVCGSTRN
NESESTLDLE GFQNPTAKEC EGLATLDNKA DLDGESTEGT EELEDSLNHF THSVQGQTSE
MIPSDEEEED DEEEEEEEEP RLTINQREDE DGMANEDELD NTYTGSGDED ALSEEDDELG
EAAKYEDVKE CGKHVERALL VELNKISLKE ENVCEEKNSP VDQSDFFYEF SKLIFTKGKS
PTVVCSLCKR EGHLKKDCPE DFKRIQLEPL PPLTPKFLNI LDQVCIQCYK DFSPTIIEDQ
AREHIRQNLE SFIRQDFPGT KLSLFGSSKN GFGFKQSDLD VCMTINGLET AEGLDCVRTI
EELARVLRKH SGLRNILPIT TAKVPIVKFF HLRSGLEVDI SLYNTLALHN TRLLSAYSAI
DPRVKYLCYT MKVFTKMCDI GDASRGSLSS YAYTLMVLYF LQQRNPPVIP VLQEIYKGEK
KPEIFVDGWN IYFFDQIDEL PTYWSECGKN TESVGQLWLG LLRFYTEEFD FKEHVISIRR
KSLLTTFKKQ WTSKYIVIED PFDLNHNLGA GLSRKMTNFI MKAFINGRRV FGIPVKGFPK
DYPSKMEYFF DPDVLTEGEL APNDRCCRIC GKIGHFMKDC PMRRKVRRRR DQEDALNQRY
PENKEKRSKE DKEIHNKYTE REVSTKEDKP IQCTPQKAKP MRAAADLGRE KILRPPVEKW
KRQDDKDLRE KRCFICGREG HIKKECPQFK GSSGSLSSKY MTQGKASAKR TQQES
